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MAP kinase-activated protein kinase 2 (MAPK-activated protein kinase 2) (MAPKAP kinase 2) (MAPKAP-K2) (MAPKAPK-2) (MK-2) (MK2) (EC 2.7.11.1)

 MAPK2_HUMAN             Reviewed;         400 AA.
P49137; Q5SY30; Q5SY41; Q8IYD6;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 185.
RecName: Full=MAP kinase-activated protein kinase 2;
Short=MAPK-activated protein kinase 2;
Short=MAPKAP kinase 2;
Short=MAPKAP-K2;
Short=MAPKAPK-2;
Short=MK-2;
Short=MK2;
EC=2.7.11.1;
Name=MAPKAPK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8179591; DOI=10.1006/bbrc.1994.1566;
Zu Y.-L., Wu F., Gilchrist A., Ai Y., Labadia M.E., Huang C.K.;
"The primary structure of a human MAP kinase activated protein kinase
2.";
Biochem. Biophys. Res. Commun. 200:1118-1124(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-400 (ISOFORM 1), AND FUNCTION.
PubMed=8280084; DOI=10.1042/bj2960843;
Stokoe D., Caudwell B., Cohen P.T.W., Cohen P.;
"The substrate specificity and structure of mitogen-activated protein
(MAP) kinase-activated protein kinase-2.";
Biochem. J. 296:843-849(1993).
[6]
FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=8093612;
Jakob U., Gaestel M., Engel K., Buchner J.;
"Small heat shock proteins are molecular chaperones.";
J. Biol. Chem. 268:1517-1520(1993).
[7]
PHOSPHORYLATION AT SER-9; THR-25; THR-222; SER-272 AND THR-334, AND
MUTAGENESIS OF ASP-207; THR-222; SER-272 AND THR-334.
PubMed=8846784;
Ben-Levy R., Leighton I.A., Doza Y.N., Attwood P., Morrice N.,
Marshall C.J., Cohen P.;
"Identification of novel phosphorylation sites required for activation
of MAPKAP kinase-2.";
EMBO J. 14:5920-5930(1995).
[8]
CATALYTIC ACTIVITY, AND FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=8774846; DOI=10.1016/0014-5793(96)00816-2;
Clifton A.D., Young P.R., Cohen P.;
"A comparison of the substrate specificity of MAPKAP kinase-2 and
MAPKAP kinase-3 and their activation by cytokines and cellular
stress.";
FEBS Lett. 392:209-214(1996).
[9]
FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=10383393; DOI=10.1074/jbc.274.27.18947;
Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G.,
Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.;
"Regulation of Hsp27 oligomerization, chaperone function, and
protective activity against oxidative stress/tumor necrosis factor
alpha by phosphorylation.";
J. Biol. Chem. 274:18947-18956(1999).
[10]
FUNCTION IN PHOSPHORYLATION OF HNRNPA0.
PubMed=12456657; DOI=10.1093/emboj/cdf639;
Rousseau S., Morrice N., Peggie M., Campbell D.G., Gaestel M.,
Cohen P.;
"Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-
K2 and its interaction with cytokine mRNAs.";
EMBO J. 21:6505-6514(2002).
[11]
FUNCTION IN PHOSPHORYLATION OF LOX5.
PubMed=11844797; DOI=10.1074/jbc.M111945200;
Werz O., Szellas D., Steinhilber D., Radmark O.;
"Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-
271 by MAPK-activated protein kinase 2 (MK2).";
J. Biol. Chem. 277:14793-14800(2002).
[12]
FUNCTION IN PHOSPHORYLATION OF PABPC1.
PubMed=12565831; DOI=10.1016/S0006-291X(03)00015-9;
Bollig F., Winzen R., Gaestel M., Kostka S., Resch K., Holtmann H.;
"Affinity purification of ARE-binding proteins identifies polyA-
binding protein 1 as a potential substrate in MK2-induced mRNA
stabilization.";
Biochem. Biophys. Res. Commun. 301:665-670(2003).
[13]
FUNCTION.
PubMed=14499342; DOI=10.1016/S0898-6568(03)00074-3;
Coxon P.Y., Rane M.J., Uriarte S., Powell D.W., Singh S., Butt W.,
Chen Q., McLeish K.R.;
"MAPK-activated protein kinase-2 participates in p38 MAPK-dependent
and ERK-dependent functions in human neutrophils.";
Cell. Signal. 15:993-1001(2003).
[14]
FUNCTION IN PHOSPHORYLATION OF ELAVL1, AND MUTAGENESIS OF LYS-93;
THR-222 AND THR-334.
PubMed=14517288; DOI=10.1128/MCB.23.20.7177-7188.2003;
Tran H., Maurer F., Nagamine Y.;
"Stabilization of urokinase and urokinase receptor mRNAs by HuR is
linked to its cytoplasmic accumulation induced by activated mitogen-
activated protein kinase-activated protein kinase 2.";
Mol. Cell. Biol. 23:7177-7188(2003).
[15]
FUNCTION IN PHOSPHORYLATION OF ZFP36, AND MUTAGENESIS OF THR-222 AND
THR-334.
PubMed=15014438; DOI=10.1038/sj.emboj.7600163;
Stoecklin G., Stubbs T., Kedersha N., Wax S., Rigby W.F.,
Blackwell T.K., Anderson P.;
"MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule
association and ARE-mRNA decay.";
EMBO J. 23:1313-1324(2004).
[16]
INTERACTION WITH PHC2.
PubMed=15094067; DOI=10.1016/S0014-5793(04)00351-5;
Yannoni Y.M., Gaestel M., Lin L.L.;
"P66(ShcA) interacts with MAPKAP kinase 2 and regulates its
activity.";
FEBS Lett. 564:205-211(2004).
[17]
FUNCTION IN PHOSPHORYLATION OF CDC25B AND CDC25C.
PubMed=15629715; DOI=10.1016/j.molcel.2004.11.021;
Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.;
"MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the
G2/M transition and S phase progression in response to UV
irradiation.";
Mol. Cell 17:37-48(2005).
[18]
FUNCTION IN PHOSPHORYLATION OF LIMK1.
PubMed=16456544; DOI=10.1038/sj.emboj.7600973;
Kobayashi M., Nishita M., Mishima T., Ohashi K., Mizuno K.;
"MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced
actin remodeling and cell migration.";
EMBO J. 25:713-726(2006).
[19]
FUNCTION IN PHOSPHORYLATION OF HSF1, AND INTERACTION WITH HSF1.
PubMed=16278218; DOI=10.1074/jbc.M505822200;
Wang X., Khaleque M.A., Zhao M.J., Zhong R., Gaestel M.,
Calderwood S.K.;
"Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine
121, inhibits transcriptional activity and promotes HSP90 binding.";
J. Biol. Chem. 281:782-791(2006).
[20]
FUNCTION IN PHOSPHORYLATION OF LSP1.
PubMed=17481585; DOI=10.1016/j.bbrc.2007.04.104;
Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K.,
Madri J.A.;
"MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil
polarization.";
Biochem. Biophys. Res. Commun. 358:170-175(2007).
[21]
FUNCTION IN PHOSPHORYLATION OF TAB3.
PubMed=18021073; DOI=10.1042/BJ20071149;
Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N.,
Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L.,
Ghosh S., Cohen P.;
"Roles for TAB1 in regulating the IL-1-dependent phosphorylation of
the TAB3 regulatory subunit and activity of the TAK1 complex.";
Biochem. J. 409:711-722(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
FUNCTION IN PHOSPHORYLATION OF HNRNPA0 AND PARN, AND SUBCELLULAR
LOCATION.
PubMed=20932473; DOI=10.1016/j.molcel.2010.09.018;
Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S.,
van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A.,
Yaffe M.B.;
"DNA damage activates a spatially distinct late cytoplasmic cell-cycle
checkpoint network controlled by MK2-mediated RNA stabilization.";
Mol. Cell 40:34-49(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
SUMOYLATION AT LYS-353, AND MUTAGENESIS OF LYS-353.
PubMed=21131586; DOI=10.1182/blood-2010-08-302281;
Chang E., Heo K.S., Woo C.H., Lee H., Le N.T., Thomas T.N.,
Fujiwara K., Abe J.;
"MK2 SUMOylation regulates actin filament remodeling and subsequent
migration in endothelial cells by inhibiting MK2 kinase and HSP27
phosphorylation.";
Blood 117:2527-2537(2011).
[26]
REVIEW.
PubMed=18508601; DOI=10.2741/3095;
Ronkina N., Kotlyarov A., Gaestel M.;
"MK2 and MK3--a pair of isoenzymes?";
Front. Biosci. 13:5511-5521(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
FUNCTION.
PubMed=26616734; DOI=10.1038/ncomms10075;
Tollenaere M.A., Villumsen B.H., Blasius M., Nielsen J.C.,
Wagner S.A., Bartek J., Beli P., Mailand N., Bekker-Jensen S.;
"p38- and MK2-dependent signalling promotes stress-induced centriolar
satellite remodelling via 14-3-3-dependent sequestration of
CEP131/AZI1.";
Nat. Commun. 6:10075-10075(2015).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ADP AND
STAUROSPORINE, AND CATALYTIC ACTIVITY.
PubMed=12171911; DOI=10.1074/jbc.C200418200;
Meng W., Swenson L.L., Fitzgibbon M.J., Hayakawa K., Ter Haar E.,
Behrens A.E., Fulghum J.R., Lippke J.A.;
"Structure of mitogen-activated protein kinase-activated protein
(MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase
activation with nuclear export.";
J. Biol. Chem. 277:37401-37405(2002).
[31]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=12791252; DOI=10.1016/S0969-2126(03)00092-3;
Underwood K.W., Parris K.D., Federico E., Mosyak L., Czerwinski R.M.,
Shane T., Taylor M., Svenson K., Liu Y., Hsiao C.L., Wolfrom S.,
Maguire M., Malakian K., Telliez J.B., Lin L.L., Kriz R.W., Seehra J.,
Somers W.S., Stahl M.L.;
"Catalytically active MAP KAP kinase 2 structures in complex with
staurosporine and ADP reveal differences with the autoinhibited
enzyme.";
Structure 11:627-636(2003).
[32]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 41-364 IN COMPLEX WITH
CARBOLINE-BASED INHIBITORS.
PubMed=17576063; DOI=10.1016/j.bmcl.2007.05.101;
Wu J.P., Wang J., Abeywardane A., Andersen D., Emmanuel M.,
Gautschi E., Goldberg D.R., Kashem M.A., Lukas S., Mao W., Martin L.,
Morwick T., Moss N., Pargellis C., Patel U.R., Patnaude L., Peet G.W.,
Skow D., Snow R.J., Ward Y., Werneburg B., White A.;
"The discovery of carboline analogs as potent MAPKAP-K2 inhibitors.";
Bioorg. Med. Chem. Lett. 17:4664-4669(2007).
[33]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH MAPK14, AND
INTERACTION WITH MAPK14.
PubMed=17255097; DOI=10.1074/jbc.M611165200;
ter Haar E., Prabhakar P., Liu X., Lepre C.;
"Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer.";
J. Biol. Chem. 282:9733-9739(2007).
[34]
ERRATUM.
ter Haar E., Prabhakar P., Liu X., Lepre C.;
J. Biol. Chem. 282:14684-14684(2007).
[35]
X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 45-371 IN COMPLEX WITH
PYRROLOPYRIDINE INHIBITORS.
PubMed=17480064; DOI=10.1021/jm0611004;
Anderson D.R., Meyers M.J., Vernier W.F., Mahoney M.W.,
Kurumbail R.G., Caspers N., Poda G.I., Schindler J.F., Reitz D.B.,
Mourey R.J.;
"Pyrrolopyridine inhibitors of mitogen-activated protein kinase-
activated protein kinase 2 (MK-2).";
J. Med. Chem. 50:2647-2654(2007).
[36]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 41-364 IN COMPLEX WITH
PYRROLOPYRIDINE INHIBITOR.
PubMed=17449059; DOI=10.1016/j.jmb.2007.03.004;
Hillig R.C., Eberspaecher U., Monteclaro F., Huber M., Nguyen D.,
Mengel A., Muller-Tiemann B., Egner U.;
"Structural basis for a high affinity inhibitor bound to protein
kinase MK2.";
J. Mol. Biol. 369:735-745(2007).
[37]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 47-400 IN COMPLEX WITH
MAPK14, AND INTERACTION WITH MAPK14.
PubMed=17395714; DOI=10.1073/pnas.0701679104;
White A., Pargellis C.A., Studts J.M., Werneburg B.G., Farmer B.T. II;
"Molecular basis of MAPK-activated protein kinase 2:p38 assembly.";
Proc. Natl. Acad. Sci. U.S.A. 104:6353-6358(2007).
[38]
VARIANTS [LARGE SCALE ANALYSIS] GLY-173 AND SER-361.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Stress-activated serine/threonine-protein kinase
involved in cytokine production, endocytosis, reorganization of
the cytoskeleton, cell migration, cell cycle control, chromatin
remodeling, DNA damage response and transcriptional regulation.
Following stress, it is phosphorylated and activated by MAP kinase
p38-alpha/MAPK14, leading to phosphorylation of substrates.
Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S,
where Hyd is a large hydrophobic residue. Phosphorylates ALOX5,
CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18,
KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and
TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with
HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding
and transactivation activities (PubMed:16278218). Mediates
phosphorylation of HSP27/HSPB1 in response to stress, leading to
the dissociation of HSP27/HSPB1 from large small heat-shock
protein (sHsps) oligomers and impairment of their chaperone
activities and ability to protect against oxidative stress
effectively. Involved in inflammatory response by regulating tumor
necrosis factor (TNF) and IL6 production post-transcriptionally:
acts by phosphorylating AU-rich elements (AREs)-binding proteins
ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation
of the stability and translation of TNF and IL6 mRNAs.
Phosphorylation of TTP/ZFP36, a major post-transcriptional
regulator of TNF, promotes its binding to 14-3-3 proteins and
reduces its ARE mRNA affinity, leading to inhibition of dependent
degradation of ARE-containing transcripts. Phosphorylates CEP131
in response to cellular stress induced by ultraviolet irradiation
which promotes binding of CEP131 to 14-3-3 proteins and inhibits
formation of novel centriolar satellites (PubMed:26616734). Also
involved in late G2/M checkpoint following DNA damage through a
process of post-transcriptional mRNA stabilization: following DNA
damage, relocalizes from nucleus to cytoplasm and phosphorylates
HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA.
Involved in toll-like receptor signaling pathway (TLR) in
dendritic cells: required for acute TLR-induced macropinocytosis
by phosphorylating and activating RPS6KA3.
{ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:11844797,
ECO:0000269|PubMed:12456657, ECO:0000269|PubMed:12565831,
ECO:0000269|PubMed:14499342, ECO:0000269|PubMed:14517288,
ECO:0000269|PubMed:15014438, ECO:0000269|PubMed:15629715,
ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:16456544,
ECO:0000269|PubMed:17481585, ECO:0000269|PubMed:18021073,
ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:26616734,
ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8280084,
ECO:0000269|PubMed:8774846}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:12171911, ECO:0000269|PubMed:8774846}.
-!- ENZYME REGULATION: Activated following phosphorylation by p38-
alpha/MAPK14 following various stresses. Inhibited following
sumoylation. Specifically inhibited by pyrrolopyridine inhibitors.
-!- SUBUNIT: Heterodimer with p38-alpha/MAPK14; this heterodimer forms
a stable complex: molecules are positioned 'face to face' so that
the ATP-binding sites of both kinases are at the heterodimer
interface (PubMed:12171911, PubMed:17576063, PubMed:17255097,
PubMed:17480064, PubMed:17449059, PubMed:17395714). Interacts with
PHC2 (PubMed:15094067). Interacts with HSF1 (PubMed:16278218).
{ECO:0000269|PubMed:12171911, ECO:0000269|PubMed:15094067,
ECO:0000269|PubMed:16278218, ECO:0000269|PubMed:17255097,
ECO:0000269|PubMed:17395714, ECO:0000269|PubMed:17449059,
ECO:0000269|PubMed:17480064, ECO:0000269|PubMed:17576063}.
-!- INTERACTION:
Q00613:HSF1; NbExp=5; IntAct=EBI-993299, EBI-719620;
P04792:HSPB1; NbExp=3; IntAct=EBI-993299, EBI-352682;
Q16539:MAPK14; NbExp=7; IntAct=EBI-993299, EBI-73946;
P47811:Mapk14 (xeno); NbExp=2; IntAct=EBI-15629963, EBI-298727;
Q9QWH1:Phc2 (xeno); NbExp=2; IntAct=EBI-993299, EBI-642357;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20932473}.
Nucleus {ECO:0000269|PubMed:20932473}. Note=Phosphorylation and
subsequent activation releases the autoinhibitory helix, resulting
in the export from the nucleus into the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P49137-1; Sequence=Displayed;
Note=Has a nuclear localization signal.;
Name=2;
IsoId=P49137-2; Sequence=VSP_004910;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined.
-!- PTM: Sumoylation inhibits the protein kinase activity.
{ECO:0000269|PubMed:21131586}.
-!- PTM: Phosphorylated and activated by MAP kinase p38-alpha/MAPK14
at Thr-222, Ser-272 and Thr-334. {ECO:0000269|PubMed:8846784}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAPKAPK2ID41295ch1q32.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U12779; AAA20851.1; -; mRNA.
EMBL; AL591846; CAI13543.1; -; Genomic_DNA.
EMBL; AL591846; CAI13544.1; -; Genomic_DNA.
EMBL; CH471100; EAW93526.1; -; Genomic_DNA.
EMBL; CH471100; EAW93529.1; -; Genomic_DNA.
EMBL; BC036060; AAH36060.2; -; mRNA.
EMBL; BC052584; AAH52584.1; -; mRNA.
EMBL; X75346; CAA53094.1; -; mRNA.
CCDS; CCDS1466.1; -. [P49137-2]
CCDS; CCDS31001.1; -. [P49137-1]
PIR; JC2204; JC2204.
PIR; S39793; S39793.
RefSeq; NP_004750.1; NM_004759.4. [P49137-2]
RefSeq; NP_116584.2; NM_032960.3. [P49137-1]
UniGene; Hs.643566; -.
UniGene; Hs.713747; -.
PDB; 1KWP; X-ray; 2.80 A; A/B=1-400.
PDB; 1NXK; X-ray; 2.70 A; A/B/C/D=1-400.
PDB; 1NY3; X-ray; 3.00 A; A=1-400.
PDB; 2JBO; X-ray; 3.10 A; A=41-364.
PDB; 2JBP; X-ray; 3.31 A; A/B/C/D/E/F/G/H/I/J/K/L=41-364.
PDB; 2OKR; X-ray; 2.00 A; C/F=370-393.
PDB; 2ONL; X-ray; 4.00 A; C/D=1-400.
PDB; 2OZA; X-ray; 2.70 A; A=47-400.
PDB; 2P3G; X-ray; 3.80 A; X=45-371.
PDB; 2PZY; X-ray; 2.90 A; A/B/C/D=41-364.
PDB; 3A2C; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=41-364.
PDB; 3FPM; X-ray; 3.30 A; A=41-364.
PDB; 3FYJ; X-ray; 3.80 A; X=45-371.
PDB; 3FYK; X-ray; 3.50 A; X=45-371.
PDB; 3GOK; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=41-364.
PDB; 3KA0; X-ray; 2.90 A; A=47-366.
PDB; 3KC3; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=41-364.
PDB; 3KGA; X-ray; 2.55 A; A=47-364.
PDB; 3M2W; X-ray; 2.41 A; A=47-364.
PDB; 3M42; X-ray; 2.68 A; A=47-364.
PDB; 3R2B; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=47-364.
PDB; 3R2Y; X-ray; 3.00 A; A=46-364.
PDB; 3R30; X-ray; 3.20 A; A=46-364.
PDB; 3WI6; X-ray; 2.99 A; A/B/C/D/E/F=41-364.
PDB; 4TYH; X-ray; 3.00 A; A=51-400.
PDBsum; 1KWP; -.
PDBsum; 1NXK; -.
PDBsum; 1NY3; -.
PDBsum; 2JBO; -.
PDBsum; 2JBP; -.
PDBsum; 2OKR; -.
PDBsum; 2ONL; -.
PDBsum; 2OZA; -.
PDBsum; 2P3G; -.
PDBsum; 2PZY; -.
PDBsum; 3A2C; -.
PDBsum; 3FPM; -.
PDBsum; 3FYJ; -.
PDBsum; 3FYK; -.
PDBsum; 3GOK; -.
PDBsum; 3KA0; -.
PDBsum; 3KC3; -.
PDBsum; 3KGA; -.
PDBsum; 3M2W; -.
PDBsum; 3M42; -.
PDBsum; 3R2B; -.
PDBsum; 3R2Y; -.
PDBsum; 3R30; -.
PDBsum; 3WI6; -.
PDBsum; 4TYH; -.
ProteinModelPortal; P49137; -.
SMR; P49137; -.
BioGrid; 114683; 61.
DIP; DIP-35671N; -.
ELM; P49137; -.
IntAct; P49137; 15.
MINT; MINT-1539725; -.
STRING; 9606.ENSP00000356070; -.
BindingDB; P49137; -.
ChEMBL; CHEMBL2208; -.
DrugBank; DB02010; Staurosporine.
GuidetoPHARMACOLOGY; 2094; -.
iPTMnet; P49137; -.
PhosphoSitePlus; P49137; -.
BioMuta; MAPKAPK2; -.
DMDM; 1346538; -.
EPD; P49137; -.
MaxQB; P49137; -.
PaxDb; P49137; -.
PeptideAtlas; P49137; -.
PRIDE; P49137; -.
DNASU; 9261; -.
Ensembl; ENST00000294981; ENSP00000294981; ENSG00000162889. [P49137-2]
Ensembl; ENST00000367103; ENSP00000356070; ENSG00000162889. [P49137-1]
GeneID; 9261; -.
KEGG; hsa:9261; -.
UCSC; uc001hel.3; human. [P49137-1]
CTD; 9261; -.
DisGeNET; 9261; -.
EuPathDB; HostDB:ENSG00000162889.10; -.
GeneCards; MAPKAPK2; -.
HGNC; HGNC:6887; MAPKAPK2.
HPA; CAB010297; -.
HPA; HPA045556; -.
HPA; HPA063708; -.
HPA; HPA064435; -.
MIM; 602006; gene.
neXtProt; NX_P49137; -.
OpenTargets; ENSG00000162889; -.
PharmGKB; PA30631; -.
eggNOG; KOG0604; Eukaryota.
eggNOG; ENOG410XP8F; LUCA.
GeneTree; ENSGT00900000140876; -.
HOGENOM; HOG000233031; -.
HOVERGEN; HBG106948; -.
InParanoid; P49137; -.
KO; K04443; -.
OMA; CRHIVNI; -.
OrthoDB; EOG091G14PL; -.
PhylomeDB; P49137; -.
TreeFam; TF312891; -.
BioCyc; MetaCyc:HS08751-MONOMER; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-199920; CREB phosphorylation.
Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
SignaLink; P49137; -.
SIGNOR; P49137; -.
ChiTaRS; MAPKAPK2; human.
EvolutionaryTrace; P49137; -.
GeneWiki; MAPKAPK2; -.
GenomeRNAi; 9261; -.
PRO; PR:P49137; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162889; -.
CleanEx; HS_MAPKAPK2; -.
Genevisible; P49137; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
GO; GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
GO; GO:0044351; P:macropinocytosis; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:ProtInc.
GO; GO:0038066; P:p38MAPK cascade; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0032675; P:regulation of interleukin-6 production; ISS:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0032680; P:regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0034097; P:response to cytokine; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0006950; P:response to stress; IDA:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
Gene3D; 4.10.1170.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR027442; MAPKAPK_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; DNA damage; Isopeptide bond; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 400 MAP kinase-activated protein kinase 2.
/FTId=PRO_0000086288.
DOMAIN 64 325 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 70 78 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 139 141 Staurosporine binding.
REGION 328 364 Autoinhibitory helix. {ECO:0000250}.
REGION 366 390 p38 MAPK-binding site.
MOTIF 356 365 Nuclear export signal (NES).
MOTIF 371 374 Bipartite nuclear localization signal 1.
MOTIF 385 389 Bipartite nuclear localization signal 2.
COMPBIAS 10 40 Pro-rich.
COMPBIAS 35 40 Poly-Pro.
ACT_SITE 186 186 Proton acceptor.
BINDING 93 93 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000269|PubMed:8846784}.
MOD_RES 25 25 Phosphothreonine.
{ECO:0000269|PubMed:8846784}.
MOD_RES 222 222 Phosphothreonine; by MAPK14.
{ECO:0000269|PubMed:8846784}.
MOD_RES 272 272 Phosphoserine; by MAPK14.
{ECO:0000269|PubMed:8846784}.
MOD_RES 328 328 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 334 334 Phosphothreonine; by MAPK14.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:8846784}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:21131586}.
VAR_SEQ 354 400 EEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARALE
AAALAH -> GCLHDKNSDQATWLTRL (in isoform
2). {ECO:0000303|PubMed:8179591}.
/FTId=VSP_004910.
VARIANT 173 173 A -> G (in dbSNP:rs35671930).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040753.
VARIANT 361 361 A -> S (in dbSNP:rs55894011).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040754.
MUTAGEN 93 93 K->R: Kinase defective mutant, abolishes
activity. {ECO:0000269|PubMed:14517288}.
MUTAGEN 207 207 D->A: Kinase defective mutant, abolishes
activity. {ECO:0000269|PubMed:8846784}.
MUTAGEN 222 222 T->A: Strong decrease in kinase activity.
{ECO:0000269|PubMed:14517288,
ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:8846784}.
MUTAGEN 222 222 T->D: Mimicks phosphorylation state,
leading to slight increase of basal
kinase activity.
{ECO:0000269|PubMed:14517288,
ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:8846784}.
MUTAGEN 222 222 T->E: Mimicks phosphorylation state and
constitutive protein kinase activity;
when associated with E-334.
{ECO:0000269|PubMed:14517288,
ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:8846784}.
MUTAGEN 272 272 S->A: Strong decrease in kinase activity.
{ECO:0000269|PubMed:8846784}.
MUTAGEN 272 272 S->D: Mimicks phosphorylation state,
leading to slight increase of basal
kinase activity.
{ECO:0000269|PubMed:8846784}.
MUTAGEN 334 334 T->A: Slight decrease in kinase activity.
{ECO:0000269|PubMed:14517288,
ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:8846784}.
MUTAGEN 334 334 T->D,E: Mimicks phosphorylation state,
leading to elevated basal kinase
activity. {ECO:0000269|PubMed:14517288,
ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:8846784}.
MUTAGEN 334 334 T->E: Mimicks phosphorylation state and
constitutive protein kinase activity;
when associated with E-222.
{ECO:0000269|PubMed:14517288,
ECO:0000269|PubMed:15014438,
ECO:0000269|PubMed:8846784}.
MUTAGEN 353 353 K->R: Induces decreased sumoylation and
increase in protein kinase activity.
{ECO:0000269|PubMed:21131586}.
CONFLICT 116 116 H -> D (in Ref. 5; CAA53094).
{ECO:0000305}.
CONFLICT 247 248 WS -> LV (in Ref. 5; CAA53094).
{ECO:0000305}.
HELIX 45 47 {ECO:0000244|PDB:1NXK}.
STRAND 48 50 {ECO:0000244|PDB:1NXK}.
HELIX 59 61 {ECO:0000244|PDB:3M2W}.
STRAND 63 73 {ECO:0000244|PDB:3M2W}.
STRAND 76 83 {ECO:0000244|PDB:3M2W}.
TURN 84 86 {ECO:0000244|PDB:3M2W}.
STRAND 89 96 {ECO:0000244|PDB:3M2W}.
HELIX 99 111 {ECO:0000244|PDB:3M2W}.
STRAND 114 117 {ECO:0000244|PDB:3FYK}.
STRAND 120 128 {ECO:0000244|PDB:3M2W}.
STRAND 131 138 {ECO:0000244|PDB:3M2W}.
STRAND 143 145 {ECO:0000244|PDB:1NXK}.
HELIX 146 152 {ECO:0000244|PDB:3M2W}.
HELIX 160 179 {ECO:0000244|PDB:3M2W}.
HELIX 189 191 {ECO:0000244|PDB:3M2W}.
STRAND 192 198 {ECO:0000244|PDB:3M2W}.
STRAND 203 205 {ECO:0000244|PDB:3M2W}.
STRAND 212 214 {ECO:0000244|PDB:3WI6}.
STRAND 228 230 {ECO:0000244|PDB:3FPM}.
HELIX 232 234 {ECO:0000244|PDB:1NXK}.
HELIX 239 242 {ECO:0000244|PDB:3M2W}.
HELIX 243 258 {ECO:0000244|PDB:3M2W}.
STRAND 264 266 {ECO:0000244|PDB:4TYH}.
STRAND 267 269 {ECO:0000244|PDB:1KWP}.
HELIX 275 281 {ECO:0000244|PDB:1NXK}.
STRAND 283 285 {ECO:0000244|PDB:2OZA}.
HELIX 288 291 {ECO:0000244|PDB:3M2W}.
HELIX 296 305 {ECO:0000244|PDB:3M2W}.
TURN 310 312 {ECO:0000244|PDB:3M2W}.
HELIX 316 320 {ECO:0000244|PDB:3M2W}.
HELIX 323 326 {ECO:0000244|PDB:3M2W}.
HELIX 328 330 {ECO:0000244|PDB:3M2W}.
STRAND 335 337 {ECO:0000244|PDB:3M42}.
HELIX 338 344 {ECO:0000244|PDB:3M2W}.
HELIX 346 348 {ECO:0000244|PDB:3M2W}.
HELIX 349 363 {ECO:0000244|PDB:3M2W}.
TURN 375 377 {ECO:0000244|PDB:2OKR}.
HELIX 381 389 {ECO:0000244|PDB:2OKR}.
SEQUENCE 400 AA; 45568 MW; E4EFFF11CCF288DC CRC64;
MLSNSQGQSP PVPFPAPAPP PQPPTPALPH PPAQPPPPPP QQFPQFHVKS GLQIKKNAII
DDYKVTSQVL GLGINGKVLQ IFNKRTQEKF ALKMLQDCPK ARREVELHWR ASQCPHIVRI
VDVYENLYAG RKCLLIVMEC LDGGELFSRI QDRGDQAFTE REASEIMKSI GEAIQYLHSI
NIAHRDVKPE NLLYTSKRPN AILKLTDFGF AKETTSHNSL TTPCYTPYYV APEVLGPEKY
DKSCDMWSLG VIMYILLCGY PPFYSNHGLA ISPGMKTRIR MGQYEFPNPE WSEVSEEVKM
LIRNLLKTEP TQRMTITEFM NHPWIMQSTK VPQTPLHTSR VLKEDKERWE DVKEEMTSAL
ATMRVDYEQI KIKKIEDASN PLLLKRRKKA RALEAAALAH


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